TLC2_ARATH
ID TLC2_ARATH Reviewed; 618 AA.
AC P92935; Q9M9E3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ADP,ATP carrier protein 2, chloroplastic;
DE AltName: Full=ADP/ATP translocase 2;
DE AltName: Full=Adenine nucleotide translocase 2;
DE Flags: Precursor;
GN Name=AATP2; OrderedLocusNames=At1g15500; ORFNames=T16N11.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9546649; DOI=10.1046/j.1432-1327.1998.2520353.x;
RA Moehlmann T., Tjaden J., Schwoeppe C., Winkler H.H., Kampfenkel K.,
RA Neuhaus H.E.;
RT "Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana
RT L. -- molecular characterisation and comparative structural analysis of
RT similar ATP/ADP translocators from plastids and Rickettsia prowazekii.";
RL Eur. J. Biochem. 252:353-359(1998).
RN [2]
RP SEQUENCE REVISION.
RA Neuhaus E.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-77, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc (TC 2.A.12.2)
CC family. {ECO:0000305}.
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DR EMBL; X94626; CAA64329.2; -; mRNA.
DR EMBL; AC013453; AAF71976.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29330.1; -; Genomic_DNA.
DR EMBL; AY081350; AAL91239.1; -; mRNA.
DR EMBL; AY128844; AAM91244.1; -; mRNA.
DR EMBL; AY084374; AAM60955.1; -; mRNA.
DR PIR; G86288; G86288.
DR RefSeq; NP_173003.1; NM_101419.3.
DR AlphaFoldDB; P92935; -.
DR BioGRID; 23360; 5.
DR IntAct; P92935; 3.
DR STRING; 3702.AT1G15500.1; -.
DR TCDB; 2.A.12.1.19; the atp:adp antiporter (aaa) family.
DR iPTMnet; P92935; -.
DR PaxDb; P92935; -.
DR PRIDE; P92935; -.
DR ProteomicsDB; 232427; -.
DR EnsemblPlants; AT1G15500.1; AT1G15500.1; AT1G15500.
DR GeneID; 838120; -.
DR Gramene; AT1G15500.1; AT1G15500.1; AT1G15500.
DR KEGG; ath:AT1G15500; -.
DR Araport; AT1G15500; -.
DR TAIR; locus:2196588; AT1G15500.
DR eggNOG; ENOG502QSRY; Eukaryota.
DR HOGENOM; CLU_023964_0_0_1; -.
DR InParanoid; P92935; -.
DR OMA; HPNTIDY; -.
DR OrthoDB; 1270398at2759; -.
DR PhylomeDB; P92935; -.
DR BioCyc; MetaCyc:AT1G15500-MON; -.
DR PRO; PR:P92935; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92935; baseline and differential.
DR Genevisible; P92935; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR InterPro; IPR004667; ADP_ATP_car_bac_type.
DR PANTHER; PTHR31187; PTHR31187; 1.
DR Pfam; PF03219; TLC; 1.
DR TIGRFAMs; TIGR00769; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chloroplast; Membrane; Nucleotide-binding;
KW Plastid; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 77..618
FT /note="ADP,ATP carrier protein 2, chloroplastic"
FT /id="PRO_0000034360"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 586..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 618 AA; 67530 MW; B2D49E77F17A887A CRC64;
MEGLIQTRGI LSLPAKPIGV RRLLQPSHGL KQRLFTTNLP ALSLSSNGHK KFQAFQQIPL
GISVSHKERS RGFICKAEAA AAGGGNVFDE GDTAAMAVSP KIFGVEVTTL KKIVPLGLMF
FCILFNYTIL RDTKDVLVVT AKGSSAEIIP FLKTWVNLPM AIGFMLLYTK LSNVLSKKAL
FYTVIVPFIV YFGAFGFVMY PLSNLIHPEA LADKLLATLG PRFMGPLAIM RIWSFCLFYV
MAELWGSVVV SVLFWGFANQ ITTVDEAKKF YPLFGLGANV ALIFSGRTVK YFSNMRKNLG
PGVDGWAVSL KAMMSIVVGM GLAICFLYWW VNRYVPLPTR SKKKKVKPQM GTMESLKFLV
SSPYIRDLAT LVVAYGISIN LVEVTWKSKL KAQFPSPNEY SAFMGDFSTC TGIATFTMML
LSQYVFKKYG WGVAAKITPT VLLLTGVAFF SLILFGGPFA PLVAKLGMTP LLAAVYVGAL
QNIFSKSAKY SLFDPCKEMA YIPLDEDTKV KGKAAIDVVC NPLGKSGGAL IQQFMILTFG
SLANSTPYLG VILLGIVTAW LAAAKSLEGQ FNTLMSEEEL EREMERASSV KIPVVSQEDA
PSGETTSQLS EKSTPTGI
